Bilirubin glucuronyltransferase. Specific assay and kinetic studies
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چکیده
منابع مشابه
Specific Assay and Kinetic Studies by Kim
1. Bilirubin glucuronide was synthesized in vitro in a system containing a rat liver microsomal fraction, UDP-glucuronic acid, Mg2+ and bilirubin. The enzymic synthesis was accomplished without the addition of a bilirubin carrier. 2. Azobilirubin and azobilirubin glucuronide were separated by t.l.c. and paper chromatography and the measurement of the conjugate provided a specific asay for bilir...
متن کاملDetermination of bilirubin glucuronide and assay of glucuronyltransferase with bilirubin as acceptor.
1. Conjugated bilirubin is conveniently determined by coupling with the diazonium salt of ethyl anthranilate. 2. This method has been used in the development of assays for UDP-glucuronyltransferase (EC 2.4.1.17), with bilirubin as substrate, in rat liver homogenates, microsomal preparations and partly purified fractions. 3. Chromatographic analysis suggests that bilirubin monoglucuronide is the...
متن کاملAssay and properties of dititonin-activated bilirubin uridine diphosphate glucuronyltransferase from rat liver.
1. The bilirubin UDP-glucuronyltransferase assay described by Van Roy & Heirwegh (1968) has been improved. 2. Extraction of final azo-derivatives is rendered more simple and efficient by thorough emulsification and by cooling. 3. Pretreatment of homogenates and cell fractions with digitonin increases the sensitivity of the assays and gives less variable results than those with untreated prepara...
متن کاملRegulation of microsomal enzymes by phospholipids. V. Kinetic studies of hepatic uridine diphosphate-glucuronyltransferase.
A bisubstrate kinetic analysis of UDP-glucuronyltransferase (EC 2.4.1.17) has been carried out in forward and reverse directions with p-nitrophenol as aglycone. Reciprocal plots of initial rates of activity indicated that the kinetics followed a sequential mechanism. Product inhibition studies, using UDP and p-nitrophenylglucuronide as inhibitors of the forward reaction, gave a pattern of two c...
متن کاملAlbumin-Bilirubin Binding Mechanism KINETIC AND SPECTROSCOPIC STUDIES OF BINDING OF BILIRUBIN AND XANTHOBILIRUBIC ACID TO HUMAN SERUM ALBUMIN*
After binding of bilirubin to human serum albumin (1:1), a train of relaxational changes of conformation takes place. The late part of these processes, occurring in the time interval 1-500 s , has been studied by recording the changes of light absorption. Similar processes have been demonstrated after binding of fatty acid anion to the bilirubin-albumin complex as well as after a pH-jump from 6...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1971
ISSN: 0306-3283
DOI: 10.1042/bj1250027